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Conserved domains on  [gi|41055235|ref|NP_956745|]
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argininosuccinate lyase [Danio rerio]

Protein Classification

argininosuccinate lyase( domain architecture ID 10102141)

argininosuccinate lyase catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 28-460 0e+00

Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.


:

Pssm-ID: 176463 [Multi-domain]  Cd Length: 435  Bit Score: 681.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  28 SISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGDEDIHTANERRLKELIGDAAGK 107
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 108 LHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVER 187
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 188 LEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWGSMCLTHLSKMAEDLILYSTK 267
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 268 EFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQEDKEAMFDTYDTVHAVLQVA 347
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 348 TGVISTLKVNQAKMEEAL-SPDMLATDLAYHLVR-KGMPFREAHGCAGKAVYIAESKNIRLSQLTVEDLQTVSSLFDKDV 425
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 41055235 426 SSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWL 460
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 28-460 0e+00

Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.


Pssm-ID: 176463 [Multi-domain]  Cd Length: 435  Bit Score: 681.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  28 SISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGDEDIHTANERRLKELIGDAAGK 107
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 108 LHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVER 187
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 188 LEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWGSMCLTHLSKMAEDLILYSTK 267
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 268 EFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQEDKEAMFDTYDTVHAVLQVA 347
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 348 TGVISTLKVNQAKMEEAL-SPDMLATDLAYHLVR-KGMPFREAHGCAGKAVYIAESKNIRLSQLTVEDLQTVSSLFDKDV 425
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 41055235 426 SSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWL 460
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 7-464 0e+00

Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439935 [Multi-domain]  Cd Length: 462  Bit Score: 680.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   7 NKLWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGD 86
Cdd:COG0165   3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPEL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  87 EDIHTANERRLKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQ 166
Cdd:COG0165  83 EDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQ 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 167 PIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFW 246
Cdd:COG0165 163 PVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLSA 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 247 GSMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDL 326
Cdd:COG0165 243 ASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKDL 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 327 QEDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPD-MLATDLAYHLVRKGMPFREAHGCAGKAVYIAESKNIR 405
Cdd:COG0165 323 QEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGKD 402

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41055235 406 LSQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWLQAQK 464
Cdd:COG0165 403 LEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALR 461
PLN02646 PLN02646
argininosuccinate lyase
 2-464 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 675.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    2 ASSEGNKLWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFE 81
Cdd:PLN02646  11 EAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   82 IKPGDEDIHTANERRLKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTH 161
Cdd:PLN02646  91 WRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  162 MQRAQPIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVA 241
Cdd:PLN02646 171 LQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  242 EFLFWGSMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPST 321
Cdd:PLN02646 251 EFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  322 YNKDLQEDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPDML-ATDLAYHLVRKGMPFREAHGCAGKAVYIAE 400
Cdd:PLN02646 331 YNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAE 410

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055235  401 SKNIRLSQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWLQAQK 464
Cdd:PLN02646 411 SKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 9-460 0e+00

argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 129918 [Multi-domain]  Cd Length: 455  Bit Score: 600.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235     9 LWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGDED 88
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    89 IHTANERRLKELIG-DAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQP 167
Cdd:TIGR00838  81 IHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   168 IRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWG 247
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   248 SMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQ 327
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   328 EDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPD-MLATDLAYHLVRKGMPFREAHGCAGKAVYIAESKNIRL 406
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGfSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41055235   407 SQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWL 460
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
Lyase_1 pfam00206
Lyase;
12-306 1.56e-116

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 344.35  E-value: 1.56e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    12 GRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKG-EFEIKPGDEDIH 90
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    91 TANERRLKELIG-------DAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELAL-QLINTMVERAAAEIEILCPGYTHM 162
Cdd:pfam00206  81 TAVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALrQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   163 QRAQPIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDR---KLLRQELSF----DSISINSMDATG 235
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPefaELVAKELGFftglPVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055235   236 QRDFVAEFLFWGSMCLTHLSKMAEDLILYSTKEFSFINLTDAYST-GSSLMPQKKNADSLELIRSKAGRVFG 306
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 28-460 0e+00

Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.


Pssm-ID: 176463 [Multi-domain]  Cd Length: 435  Bit Score: 681.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  28 SISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGDEDIHTANERRLKELIGDAAGK 107
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 108 LHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVER 187
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 188 LEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWGSMCLTHLSKMAEDLILYSTK 267
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 268 EFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQEDKEAMFDTYDTVHAVLQVA 347
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 348 TGVISTLKVNQAKMEEAL-SPDMLATDLAYHLVR-KGMPFREAHGCAGKAVYIAESKNIRLSQLTVEDLQTVSSLFDKDV 425
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 41055235 426 SSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWL 460
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 7-464 0e+00

Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439935 [Multi-domain]  Cd Length: 462  Bit Score: 680.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   7 NKLWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGD 86
Cdd:COG0165   3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPEL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  87 EDIHTANERRLKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQ 166
Cdd:COG0165  83 EDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQ 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 167 PIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFW 246
Cdd:COG0165 163 PVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLSA 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 247 GSMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDL 326
Cdd:COG0165 243 ASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKDL 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 327 QEDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPD-MLATDLAYHLVRKGMPFREAHGCAGKAVYIAESKNIR 405
Cdd:COG0165 323 QEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGKD 402

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41055235 406 LSQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWLQAQK 464
Cdd:COG0165 403 LEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALR 461
PLN02646 PLN02646
argininosuccinate lyase
 2-464 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 675.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    2 ASSEGNKLWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFE 81
Cdd:PLN02646  11 EAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   82 IKPGDEDIHTANERRLKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTH 161
Cdd:PLN02646  91 WRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  162 MQRAQPIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVA 241
Cdd:PLN02646 171 LQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  242 EFLFWGSMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPST 321
Cdd:PLN02646 251 EFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  322 YNKDLQEDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPDML-ATDLAYHLVRKGMPFREAHGCAGKAVYIAE 400
Cdd:PLN02646 331 YNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAE 410

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055235  401 SKNIRLSQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWLQAQK 464
Cdd:PLN02646 411 SKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 7-461 0e+00

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 659.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    7 NKLWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGD 86
Cdd:PRK00855   4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   87 EDIHTANERRLKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQ 166
Cdd:PRK00855  84 EDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  167 PIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFW 246
Cdd:PRK00855 164 PVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLSA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  247 GSMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDL 326
Cdd:PRK00855 244 ASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRDL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  327 QEDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPDM-LATDLAYHLVRKGMPFREAHGCAGKAVYIAESKNIR 405
Cdd:PRK00855 324 QEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFsTATDLADYLVRKGVPFREAHEIVGKAVREAEERGVD 403

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055235  406 LSQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWLQ 461
Cdd:PRK00855 404 LADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 9-460 0e+00

argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 129918 [Multi-domain]  Cd Length: 455  Bit Score: 600.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235     9 LWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGDED 88
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    89 IHTANERRLKELIG-DAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQP 167
Cdd:TIGR00838  81 IHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   168 IRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWG 247
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   248 SMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQ 327
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   328 EDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPD-MLATDLAYHLVRKGMPFREAHGCAGKAVYIAESKNIRL 406
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGfSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41055235   407 SQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWL 460
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
PRK04833 PRK04833
argininosuccinate lyase; Provisional
 9-453 2.68e-164

argininosuccinate lyase; Provisional


Pssm-ID: 179883 [Multi-domain]  Cd Length: 455  Bit Score: 471.39  E-value: 2.68e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    9 LWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEI-KPGDE 87
Cdd:PRK04833   3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQIlASDAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   88 DIHTANERRLKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQP 167
Cdd:PRK04833  83 DIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  168 IRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWG 247
Cdd:PRK04833 163 VTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  248 SMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQ 327
Cdd:PRK04833 243 SISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  328 EDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPDML-ATDLAYHLVRKGMPFREAHGCAGKAVYIAESKNIRL 406
Cdd:PRK04833 323 EDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYAnATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 41055235  407 SQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQI 453
Cdd:PRK04833 403 EDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAI 449
PRK12308 PRK12308
argininosuccinate lyase;
9-463 3.55e-144

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 425.74  E-value: 3.55e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    9 LWGGRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDE-WSKGEFEIKPGDE 87
Cdd:PRK12308   3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEvMEDPEQILLSDAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   88 DIHTANERRLKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQP 167
Cdd:PRK12308  83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  168 IRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWG 247
Cdd:PRK12308 163 VTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  248 SMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQ 327
Cdd:PRK12308 243 SISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  328 EDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALSPDML-ATDLAYHLVRKGMPFREAHGCAGKAVYIAESKNIRL 406
Cdd:PRK12308 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYAnATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055235  407 SQLTVEDLQTVSSLFDKDVSSAWDYVKSVEQYSAPGGTSKSSVTAQIQHFKTWLQAQ 463
Cdd:PRK12308 403 EELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAAR 459
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 36-357 3.57e-134

Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.


Pssm-ID: 176461 [Multi-domain]  Cd Length: 325  Bit Score: 389.55  E-value: 3.57e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  36 WKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKGEFEIKPGDEDIHTANERRLKELIGDA-AGKLHTGRSR 114
Cdd:cd01334   1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 115 NDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVERLEDIRKR 194
Cdd:cd01334  81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 195 VNVMPLGSGAIAGNPF--DIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWGSMCLTHLSKMAEDLILYSTKEFSFI 272
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 273 NLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQEDKEAMFDTYDTVHAVLQVATGVIS 352
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320


                ....*
gi 41055235 353 TLKVN 357
Cdd:cd01334 321 GLEVN 325
Lyase_1 pfam00206
Lyase;
12-306 1.56e-116

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 344.35  E-value: 1.56e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    12 GRFVGNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLDEWSKG-EFEIKPGDEDIH 90
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    91 TANERRLKELIG-------DAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELAL-QLINTMVERAAAEIEILCPGYTHM 162
Cdd:pfam00206  81 TAVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALrQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   163 QRAQPIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDR---KLLRQELSF----DSISINSMDATG 235
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPefaELVAKELGFftglPVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055235   236 QRDFVAEFLFWGSMCLTHLSKMAEDLILYSTKEFSFINLTDAYST-GSSLMPQKKNADSLELIRSKAGRVFG 306
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 94-348 6.03e-59

Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.


Pssm-ID: 176466 [Multi-domain]  Cd Length: 231  Bit Score: 193.21  E-value: 6.03e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  94 ERRLKELIGDAAGKLH------TGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQP 167
Cdd:cd01594  17 EEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQP 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 168 IRWSHWLLSHVVAISRDVERLEDIrkrvnvmplgsgaiagnpfdidrkllrqelsfdsisinsmdatgqrdFVAEFLFWG 247
Cdd:cd01594  97 VTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALDAL 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 248 SMCLTHLSKMAEDLILYSTKEFSFINLTDA-YSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDL 326
Cdd:cd01594 130 ALAAAHLSKIAEDLRLLLSGEFGELGEPFLpGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDS 209

                       250       260
                ....*....|....*....|..
gi 41055235 327 QEDKEAMFDTYDTVHAVLQVAT 348
Cdd:cd01594 210 PSMREILADSLLLLIDALRLLL 231
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 44-396 4.00e-52

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 188.90  E-value: 4.00e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   44 KAYVKALQKASLVTQnemEQILTGLDKVLDEWSKG--EFEIKPGDEDIHTANERRLKELIG-DAAGKLHTGRSRNDQVAT 120
Cdd:PRK02186 446 EAHLVMLGDTGIVAP---ERARPLLDAHRRLRDAGfaPLLARPAPRGLYMLYEAYLIERLGeDVGGVLQTARSRNDINAT 522

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  121 DMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPL 200
Cdd:PRK02186 523 TTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPL 602

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  201 GSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWGSMCLTHLSKMAEDLILYSTKEFSFINLTDAYST 280
Cdd:PRK02186 603 GAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTG 682

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  281 GSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPstYNKDLQEDKEAMFDTYDTVHAV---LQVATGVISTLKVN 357
Cdd:PRK02186 683 GSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMNGPIAQACAAIedaAAVLVLLIDGLEAD 760

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 41055235  358 QAKMEEAL-SPDMLATDLAYHLV-RKGMPFREAHGCAGKAV 396
Cdd:PRK02186 761 QARMRAHLeDGGVSATAVAESLVvRRSISFRSAHTQVGQAI 801
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 44-414 3.01e-40

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 150.90  E-value: 3.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   44 KAYVKALQKASLVTQNEMEQILTGLDKVlDEWSKGEFEIKPGDEDIHTANERRL-KELIGDAAGKLHTGRSRNDQVATDM 122
Cdd:PRK06705  46 KAHIVMLTEENLMKKEEAKFILHALKKV-EEIPEEQLLYTEQHEDLFFLVEHLIsQEAKSDFVSNMHIGRSRNDMGVTMY 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  123 RLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGS 202
Cdd:PRK06705 125 RMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGA 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  203 GAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDFVAEFLFWGSMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTGS 282
Cdd:PRK06705 205 AALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQIS 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  283 SLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNKDLQEDKEA-MFDTYDTVHAVLQVATGVISTLKVNQAKM 361
Cdd:PRK06705 285 SIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTL 364

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41055235  362 EE-ALSPDMLATDLAYHLVRK-GMPFREAHGCAGKAVYIAESKNIRLSQLTVEDL 414
Cdd:PRK06705 365 KRrSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDV 419
PRK06389 PRK06389
argininosuccinate lyase; Provisional
 8-396 1.94e-35

argininosuccinate lyase; Provisional


Pssm-ID: 235791 [Multi-domain]  Cd Length: 434  Bit Score: 136.56  E-value: 1.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235    8 KLWGGRFV--GNTDPIMEKFNASISYDQRMWKADIKGSKAYVKALQKASLVTQNEMEQILTGLDKVLdewsKGEFEIKPG 85
Cdd:PRK06389   2 KIWSGGAGeeLENDFYDNIVKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIY----KNGIEIDLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   86 DEDIHTANERRLKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVeraAAEIEILCPGYTHMQRA 165
Cdd:PRK06389  78 LEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEIEKILYEIIKVIP---GFNLKGRLPGYTHFRQA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  166 QPIRWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDIDRKLLRQELSFDSISINSMDATGQRDF-VAEFL 244
Cdd:PRK06389 155 MPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKtIENIS 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  245 FWGSMCLTHLSKMAEDLILYSTKefSFINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLKGLPSTYNK 324
Cdd:PRK06389 235 YLISSLAVDLSRICQDIIIYYEN--GIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTGYHR 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055235  325 DLQEDKEAMFDTYDTVHAVLQVATGVISTLKVNQAKmEEALSPDMLATDLAYHLVRKGMPFREAHGCAGKAV 396
Cdd:PRK06389 313 DFQIVKDSTISFINNFERILLGLPDLLYNIKFEITN-EKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKI 383
ASL_C2 pfam14698
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ...
 369-435 6.58e-27

Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of argininosuccinate lyase.


Pssm-ID: 464268 [Multi-domain]  Cd Length: 68  Bit Score: 102.88  E-value: 6.58e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055235   369 MLATDLAYHLVRKGMPFREAHGCAGKAVYIAESKNIRLSQLTVEDLQTVSSLFDKDVSSAWDYVKSV 435
Cdd:pfam14698   2 STATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 45-389 2.67e-25

Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176467 [Multi-domain]  Cd Length: 381  Bit Score: 106.82  E-value: 2.67e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  45 AYVKALQKASLVTQ---NEMEQILTGLDKVLDEWSKGEFEIKpgdediHT--ANERRLKELIGDAAGK-LHTGRSRNDQV 118
Cdd:cd01595  20 ALAEAQAELGLIPKeaaEEIRAAADVFEIDAERIAEIEKETG------HDviAFVYALAEKCGEDAGEyVHFGATSQDIN 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 119 ATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVERLEDIRKRVNVM 198
Cdd:cd01595  94 DTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 199 ----PLGSGAIAG-NPFDIDRKLLrqelsfDSISINSMDATGQ---RDFVAEFLFWGSMCLTHLSKMAEDLILYSTKEFS 270
Cdd:cd01595 174 gisgAVGTHASLGpKGPEVEERVA------EKLGLKVPPITTQiepRDRIAELLSALALIAGTLEKIATDIRLLQRTEIG 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 271 FINL-TDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTLkglpstyNKDLQED-------KEAMFDTYDTVHA 342
Cdd:cd01595 248 EVEEpFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-------VQWHERDlsdssveRNILPDAFLLLDA 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 41055235 343 VLQVATGVISTLKVNQAKMEEALS---PDMLATDLAYHLVRKGMPFREAH 389
Cdd:cd01595 321 ALSRLQGLLEGLVVNPERMRRNLDltwGLILSEAVMMALAKKGLGRQEAY 370
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 94-389 1.47e-20

Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439786 [Multi-domain]  Cd Length: 436  Bit Score: 93.61  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  94 ERRLKELIGDAAGK-LHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSH 172
Cdd:COG0015  78 VYALKEKVGAEAGEyIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGK 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 173 WLLSHVVAISRDVERLEDIRKRVnvmPLG--SGAiAGN-------PFDIDRKLLrQELSFdsisiNSMDATGQ---RDFV 240
Cdd:COG0015 158 KLAVWAAELLRQLERLEEARERV---LVGkiGGA-VGTyaahgeaWPEVEERVA-EKLGL-----KPNPVTTQiepRDRH 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 241 AEFLFWGSMCLTHLSKMAEDLILY-ST--KEFS--FinltDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTl 315
Cdd:COG0015 228 AELFSALALIAGSLEKIARDIRLLqRTevGEVEepF----AKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEA- 302

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 316 kgLPStynkDLQED-------KEAMFDTYDTVHAVLQVATGVISTLKVNQAKME---EALSPDMLATDLAYHLVRKGMPF 385
Cdd:COG0015 303 --LAS----WHERDlsdssveRNILPDAFLLLDGALERLLKLLEGLVVNPERMRanlDLTGGLVLSEAVLMALVRRGLGR 376


                ....
gi 41055235 386 REAH 389
Cdd:COG0015 377 EEAY 380
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 95-430 2.90e-17

prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.


Pssm-ID: 176469 [Multi-domain]  Cd Length: 437  Bit Score: 83.83  E-value: 2.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  95 RRLKELIGDAAGK-LHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHW 173
Cdd:cd01597  79 KQLTAACGDAAGEyVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLK 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 174 LLSHVVAISRDVERLEDIRKRVNVMPLGsGAiAGN-------PFDIdRKLLRQELSFD--SISINSmdatgQRDFVAEFL 244
Cdd:cd01597 159 VAVWLSELLRHRERLDELRPRVLVVQFG-GA-AGTlaslgdqGLAV-QEALAAELGLGvpAIPWHT-----ARDRIAELA 230

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 245 FWGSMCLTHLSKMAEDLILYSTKEFSFINLTDAYSTG-SSLMPQKKNADSLELIRSKAGRVFGRCAGFlmtLKGLPSTYN 323
Cdd:cd01597 231 SFLALLTGTLGKIARDVYLLMQTEIGEVAEPFAKGRGgSSTMPHKRNPVGCELIVALARRVPGLAALL---LDAMVQEHE 307

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 324 KDLQEDK---EAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEALS---------PDMLAtdLAYHLVRKgmpfrEAHGC 391
Cdd:cd01597 308 RDAGAWHaewIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDltgglilseAVMMA--LAPKLGRQ-----EAHDL 380

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 41055235 392 AGKAVYIAESKNIRLSQLTVEDLQTVSSLFDKDVSSAWD 430
Cdd:cd01597 381 VYEACMRAVEEGRPLREVLLEDPEVAAYLSDEELDALLD 419
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 97-389 1.71e-14

Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).


Pssm-ID: 176464 [Multi-domain]  Cd Length: 387  Bit Score: 74.90  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  97 LKELIGDAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLS 176
Cdd:cd01360  74 IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFAL 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 177 HVVAISRDVERLEDIRKRVNVMPLgSGAIaGNPFDIDRKLlrQELSFDSISINSMDATGQ---RDFVAEFLFWGSMCLTH 253
Cdd:cd01360 154 WYAEFKRHLERLKEARERILVGKI-SGAV-GTYANLGPEV--EERVAEKLGLKPEPISTQviqRDRHAEYLSTLALIAST 229

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 254 LSKMAEDL-------ILYSTKEFsfinltDAYSTGSSLMPQKKNADSLELIRSKAgRVfgrcagflmtLKGL--PSTYNK 324
Cdd:cd01360 230 LEKIATEIrhlqrteVLEVEEPF------SKGQKGSSAMPHKRNPILSENICGLA-RV----------IRSNviPALENV 292

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 325 DLQEDKE---------AMFDTYDTVHAVLQVATGVISTLKVNQAKMEEAL---------SPDMLAtdlayhLVRKGMPFR 386
Cdd:cd01360 293 ALWHERDishssvervILPDATILLDYILRRMTRVLENLVVYPENMRRNLnltkglifsQRVLLA------LVEKGMSRE 366


                ...
gi 41055235 387 EAH 389
Cdd:cd01360 367 EAY 369
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 111-306 3.07e-13

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 71.55  E-value: 3.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  111 GRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVERLED 190
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  191 IRKRVNVMPLGSGAIaGNPFDIDRKLLRQ---ELSFDS-----ISINSMDATGQRDFVAEFLFWGSMCLTHLSKMAEDLI 262
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEYIERvvkHLAAITglplvGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 41055235  263 LYSTKE---FSFINLTdAYSTGSSLMPQKKNADSLELIRSKAGRVFG 306
Cdd:PRK13353 297 LLSSGPrtgLGEINLP-AVQPGSSIMPGKVNPVMPEVVNQIAFQVIG 342
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 62-306 1.63e-08

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 56.55  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   62 EQILTGLDKVLDEWSKGEFEIKP-----GDEDIHTANE---RRLKELIGDAAGKLH---------TGRSRNDQVATDMRl 124
Cdd:PRK14515  78 GAIAEAAQEILDGKWHDHFIVDPiqggaGTSMNMNANEviaNRALELLGMEKGDYHyispnshvnMAQSTNDAFPTAIH- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  125 wlrdgIATLKELAlQLINTM------VERAAAEIE-ILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVERLEDIRKRVNV 197
Cdd:PRK14515 157 -----IATLNALE-GLLQTMgymhdvFELKAEQFDhVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYE 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  198 MPLGSGAIaGNPFDIDRKLLRQELSF-DSIS----INS---MDATGQRDFVAEFLFWGSMCLTHLSKMAEDLILYSTKEF 269
Cdd:PRK14515 231 VNMGATAV-GTGLNADPEYIEAVVKHlAAISelplVGAedlVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPR 309

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 41055235  270 SFIN--LTDAYSTGSSLMPQKKNADSLELIRSKAGRVFG 306
Cdd:PRK14515 310 VGLAeiMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIG 348
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 111-290 2.01e-08

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 56.38  E-value: 2.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 111 GRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHWLLSHVVAISRDVERLED 190
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 191 IRKRVNVMPLGSGAI-------AGNPFDIdRKLLRQELSFD-SISINSMDATGQRD-FVAeflFWGSM--CLTHLSKMAE 259
Cdd:cd01357 213 ARERLREVNLGGTAIgtginapPGYIELV-VEKLSEITGLPlKRAENLIDATQNTDaFVE---VSGALkrLAVKLSKIAN 288

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 41055235 260 DLILYST------KEfsfINLTdAYSTGSSLMPQKKN 290
Cdd:cd01357 289 DLRLLSSgpraglGE---INLP-AVQPGSSIMPGKVN 321
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 69-389 5.67e-08

Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176471 [Multi-domain]  Cd Length: 436  Bit Score: 54.63  E-value: 5.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  69 DKVLDEWSKGEFEIkpgDEDIHTANERRLK-----------ELIGDAAGKLHTG-RSRNDQVATDMrLWLRDGIATLKEL 136
Cdd:cd03302  43 DEQIEEMKANVENI---DFEIAAAEEKKLRhdvmahvhafgLLCPAAAGIIHLGaTSCFVTDNTDL-IQIRDALDLILPK 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 137 ALQLINTMVERAAAEIEILCPGYTHMQRAQPI----RWSHWLLSHVVAISRDVERLEDIRKRVNVMPLGSGAIAGNPFDI 212
Cdd:cd03302 119 LAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTtvgkRACLWIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEG 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 213 DR-------KLLRQELSFDsisiNSMDATGQ---RDFVAEFLFWGSMCLTHLSKMAEDL-ILYSTKEfsfinLTDAYST- 280
Cdd:cd03302 199 DHdkvealdELVTKKAGFK----KVYPVTGQtysRKVDIDVLNALSSLGATAHKIATDIrLLANLKE-----VEEPFEKg 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 281 --GSSLMPQKKNADSLELIRSKAGRVFGRCAGFLMTL------KGLPSTYNK--DLQEdkeaMFDTYDTVHAVLQ-VATG 349
Cdd:cd03302 270 qiGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTAstqwfeRTLDDSANRriAIPE----AFLAADAILITLQnISEG 345

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 41055235 350 VISTLKVNQAKMEEALsPDMLATDLAYHLVRKGMPFREAH 389
Cdd:cd03302 346 LVVYPKVIERHIRQEL-PFMATENIIMAAVKAGGDRQDAH 384
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 95-290 4.23e-07

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 51.59  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235   95 RRLKELIG-DAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIRWSHW 173
Cdd:PRK05975  88 RQLRAAVGeEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADR 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  174 LLSHVVAISRDVERLEDIRKRVNVMPLGsGAIA-----GNPFDIDRKLLRQELSFdsisINSMDATGQRDFVAEFLFWGS 248
Cdd:PRK05975 168 LASWRAPLLRHRDRLEALRADVFPLQFG-GAAGtleklGGKAAAVRARLAKRLGL----EDAPQWHSQRDFIADFAHLLS 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 41055235  249 MCLTHLSKMAEDLILYSTKEfsfINLTDAYSTGSSLMPQKKN 290
Cdd:PRK05975 243 LVTGSLGKFGQDIALMAQAG---DEISLSGGGGSSAMPHKQN 281
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 103-365 3.32e-06

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 49.24  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  103 DAAGKLHTGRSRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPI----RWSHWLlshv 178
Cdd:PRK09053  97 EAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVtlglKFAGWL---- 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  179 VAISRDVERLEDIRKRVNVMPLG--SGAIA---GNPFDIDRKLLrQELsfdSISINSMDATGQRDFVAEFLFWGSMCLTH 253
Cdd:PRK09053 173 DALLRHRQRLAALRPRALVLQFGgaAGTLAslgEQALPVAQALA-AEL---QLALPALPWHTQRDRIAEFASALGLLAGT 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  254 LSKMAEDLILYSTKEFS-FINLTDAYSTGSSLMPQKKNADSLELIRSKAGRVFGRCAgflMTLKGLPSTYNKDL---QED 329
Cdd:PRK09053 249 LGKIARDVSLLMQTEVGeVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVA---TLFAAMPQEHERALggwHAE 325

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 41055235  330 KEAMFDTYDTVHAVLQVATGVISTLKVNQAKMEEAL 365
Cdd:PRK09053 326 WDTLPELACLAAGALAQMAQIVEGLEVDAARMRANL 361
aspA PRK12273
aspartate ammonia-lyase; Provisional
 113-290 2.06e-05

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 46.66  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  113 SRNDQVATDMRLWLRDGIATLKELALQLINTMVERAAAEIEILCPGYTHMQRAQPIR-------WShwllshvVAISRDV 185
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTlgqefgaYA-------VALAEDR 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  186 ERLEDIRKRVNVMPLGSGAI-------AGNPFDIDRKLlrQELSfdSISI----NSMDATGQRD-FVAeflFWGSM--CL 251
Cdd:PRK12273 215 KRLYRAAELLREVNLGATAIgtglnapPGYIELVVEKL--AEIT--GLPLvpaeDLIEATQDTGaFVE---VSGALkrLA 287

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 41055235  252 THLSKMAEDLILYST------KEfsfINLTdAYSTGSSLMPQKKN 290
Cdd:PRK12273 288 VKLSKICNDLRLLSSgpraglNE---INLP-AVQAGSSIMPGKVN 328
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 281-389 1.32e-04

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 43.09  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  281 GSSLMPQKKNADSLELIRSKAgRVFgrcAGFLMTLKGLPSTYN-KDLQEDKE---AMFDTYDTVHAVLQVATGVISTLKV 356
Cdd:PRK08937  58 GSSAMPHKRNPIGSERITGLA-RVL---RSYLVTALENVPLWHeRDLSHSSAeriALPDAFLALDYILNRFVNILENLVV 133

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 41055235  357 NQAKMEEAL---SPDMLATDLAYHLVRKGMPFREAH 389
Cdd:PRK08937 134 FPENIERNLdktLGFIATERVLLELVEKGMGREEAH 169
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 130-290 1.76e-04

aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176468 [Multi-domain]  Cd Length: 450  Bit Score: 43.95  E-value: 1.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 130 IATLKEL--AL-QLINTMVERAAAEIEILCPGYTHMQRAQPIR----WSHWllshVVAISRDVERLEDIRKRVNVMPLGS 202
Cdd:cd01596 149 LALLERLlpALeQLQDALDAKAEEFADIVKIGRTHLQDAVPLTlgqeFSGY----AAQLARDIARIEAALERLRELNLGG 224

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235 203 GAI-------AGNPFDIDRKLLRQ-ELSFDSiSINSMDATGQRD-FVAeflFWGSM--CLTHLSKMAEDLILYST----- 266
Cdd:cd01596 225 TAVgtglnapPGYAEKVAAELAELtGLPFVT-APNLFEATAAHDaLVE---VSGALktLAVSLSKIANDLRLLSSgprag 300

                       170       180
                ....*....|....*....|....*
gi 41055235 267 -KEfsfINLTdAYSTGSSLMPQKKN 290
Cdd:cd01596 301 lGE---INLP-ANQPGSSIMPGKVN 321
fumC PRK00485
fumarate hydratase; Reviewed
 111-201 3.43e-03

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 39.69  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055235  111 GRSRNDQVATDMRlwlrdgIATLKEL------ALQ-LINTMVERAAAEIEILCPGYTHMQRAQPIR----WSHWllshVV 179
Cdd:PRK00485 137 SQSSNDTFPTAMH------IAAVLAIverllpALEhLRDTLAAKAEEFADIVKIGRTHLQDATPLTlgqeFSGY----AA 206

                         90       100
                 ....*....|....*....|..
gi 41055235  180 AISRDVERLEDIRKRVNVMPLG 201
Cdd:PRK00485 207 QLEHGIERIEAALPHLYELALG 228
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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